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Mutation alters a binary bit of 1 to 0 or vice versa in the child chromosomes.
The mutation alters a Tyr to Ser in the active site of the enzyme reducing its specific activity (Dobo et al. 2010).
The mutation alters a surface protein of the virus, allowing it to dodge the immune system and infect cells throughout the bird's body, often resulting in fatal pneumonia.
On the aromatase promoter, FOXL2 binds directly to DNA at the identified forkhead site and the mutation alters a relevant protein-protein interaction (relevant to concurrent PKA and PKC signaling but not involving SF-1 or LRH-1) and in turn, alters transcription; however on the StAR promoter, FOXL2 binds DNA indirectly via SF-1, and here the mutation can not alter transcription (Fig. 7).
This mutation alters a glutamic acid in codon 172 to a lysine.
The mutation alters a GBF/Gea amino acid motif and shifts GeaA localization.
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This mutation alters an evolutionarily conserved residue in Nav1.6, one of the most abundant sodium channels in the brain.
In these mice, a single gene mutation alters an inorganic pyrophosphate transporter and is associated with spontaneous joint ankylosis [ 1].
The mutation alters an evolutionarily conserved amino acid residue, presumably leading to functional consequences as predicted by PolyPhen2.
Furthermore, the novel mutation alters an evolutionary conserved splice site and is located in the splice donor GT sequence, which is functionally important in the splicing process.
This mutation alters an invariant arginine within the putative GDP binding site, and it eliminates detectable fucosyltransferase activity, while retaining chaperone activity [ 10].
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